title: Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356.
abstract: We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent cloning and expression of the C-terminal domain in Bacillus subtilis resulted in the functional verification of the enzymatic activity.
authors.affiliation: Departamento de Química Biológica, Facultad Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
authors.forename: Mariano
authors.initials: M
authors.lastname: Prado Acosta
authors.forename: María
authors.initials: M
authors.lastname: Mercedes Palomino
authors.forename: Mariana C
authors.initials: MC
authors.lastname: Allievi
authors.forename: Carmen
authors.initials: C
authors.lastname: Sanchez Rivas
authors.forename: Sandra M
authors.initials: SM
authors.lastname: Ruzal
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D002473:Cell Wall / Q000378:metabolism; D003001:Cloning, Molecular; D007779:Lactobacillus acidophilus / Q000201:enzymology*; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: D008562:Membrane Glycoproteins; C055764:S-layer proteins; D009238:N-Acetylmuramoyl-L-alanine Amidase